Zobrazeno 61 - 70
of 86
pro vyhledávání: '"35"'
Autor:
Fiala, R., Spackova, N., Foldynová-Trantírková, S., Sponer, J., Sklenár, V., Trantirek, L., Cellular Protein Chemistry, Sub Cellular Protein Chemistry
Publikováno v:
Journal of the American Chemical Society, 133(35), 13790. American Chemical Society
In this work, a novel NMR method for the identification of preferential coordination sites between physiologically relevant counterions and nucleic acid bases is demonstrated. In this approach, the NMR cross-correlated relaxation rates between the ar
Publikováno v:
Journal of the American Chemical Society. 133(34)
Concise and protecting-group-free total syntheses of the marine oxylipins hybridalactone (1) and three members of the ecklonialactone family (2-4) were developed. They deliver these targets in optically pure form in 14 or 13 steps, respectively, in t
Publikováno v:
Journal of the American Chemical Society. 132(43)
Escherichia coli ribonucleotide reductase is an α2β2 complex that catalyzes the conversion of nucleotides to deoxynucleotides and requires a diferric-tyrosyl radical (Y(•)) cofactor to initiate catalysis. The initiation process requires long-rang
Autor:
Hiroshi Tsukube, Hiroshi Endo, Yasumasa Kanekiyo, Ken Okamoto, Jonathan P. Hill, Miki Matsukura, Satoshi Shinoda, Yasumasa Suzuki, Taizo Mori, Katsuhiko Ariga
Publikováno v:
Journal of the American Chemical Society. 132(37)
Construction of enzyme-like artificial cavities is a complex and challenging subject. Rather than synthesizing complicated host molecules, we have proposed mechanical adaptation of relatively simple hosts within dynamic media to determine the optimum
Publikováno v:
Journal of the American Chemical Society. 132(24)
E. coli ribonucleotide reductase catalyzes the reduction of nucleoside 5'-diphosphates into 2'-deoxynucleotides and is composed of two subunits: alpha2 and beta2. During turnover, a stable tyrosyl radical (Y*) at Y(122)-beta2 reversibly oxidizes C(43
Autor:
Armando Lopez, José A. Dobado, José F. Quílez del Moral, M. Mar Herrador, Alejandro F. Barrero, Victoriano Domingo, Horacio R. Dieguez, Jesús F. Arteaga
Publikováno v:
Journal of the American Chemical Society. 132(1)
Investigations detailed herein, including density functional theory (DFT) calculations, demonstrate that the formation of either alkoxy- or hydroxy-Ti(III) complexes considerably decreases the energy of activation for C-O bond homolysis. As a consequ
Autor:
Robert G. Griffin, Sylwia Kacprzak, Brian Hoffman, Erin Artin, JoAnne Stubbe, Hendrik Zipse, Debora Marcela Martino, Nicholas Lees, Martin Kaupp, Gregory J. S. Lohman, Marina Bennati, Stanislaw F. Wnuk
Publikováno v:
Journal of the American Chemical Society
The Escherichia coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleoside diphosphates to deoxynucleotides and requires a diferric-tyrosyl radical cofactor for catalysis. RNR is composed of a 1:1 complex of two homodimeric subunits:
Publikováno v:
Journal of the American Chemical Society. 130(43)
A solution state NMR study has shown that d(G4T3G4) in the presence of (15)NH4(+) ions folds into a single bimolecular G-quadruplex structure in which its G-tracts are antiparallel and the two T3 loops span along the edges of the outer G-quartets on
Autor:
Somdatta Ghosh, Abhishek Dey, Charles P. Scholes, Vladimir M. Grigoryants, Edward I. Solomon, Oleg M. Usov, Yan Sun
Publikováno v:
Journal of the American Chemical Society. 129(34)
Copper nitrite reductase (NiR) is a homotrimeric enzyme, containing a T1 copper site, which transfers electrons to the T2 catalytic site, where nitrite is reduced by one electron to nitric oxide (NO2− + 2H+ + e− → NO + H2O).1–3 Recently a sid
Publikováno v:
Journal of the American Chemical Society. 128(45)
Reaction of trans-[Ru(VI)(L)(O)(2)](2+) (1, L = 1,12-dimethyl-3,4:9,10-dibenzo-1,12-diaza-5,8-dioxacyclopentadecane, a tetradentate macrocyclic ligand with N(2)O(2) donor atoms) with nitrite in aqueous solution or in H(2)O/CH(3)CN produces the corres